Should you encounter any unexpected behaviour,
please let us know.

* NMA2BCoF *

CA strain for 2502181855492627392

--- normal mode 25 ---

This graph displays the distance variation between successive pairs of CA atoms in the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Large distance variations can be an indicator for residue pairs that support the important strain in that particular normal mode movement. Note that residue pairs between chain breaks or at flexible ends of the protein may also exhibit large CA-CA distance variations. If more than one residues ae grouped together into a rigid block (NRBL>1), CA-CA distance variations between CA atoms in the same block will be very low.

This feature is still experimental and will be further developped in the future.

CA i CA i+1 vari
MET 1 LEU 2 0.0002

LEU 2 TRP 3 0.0001

TRP 3 SER 4 0.0000

SER 4 VAL 5 0.0097

VAL 5 LEU 6 -0.0001

LEU 6 ARG 7 0.0002

ARG 7 HIS 8 0.0000

HIS 8 ILE 9 -0.0168

ILE 9 LEU 10 -0.0002

LEU 10 TRP 11 -0.0003

TRP 11 VAL 12 -0.0000

VAL 12 ALA 13 -0.0139

ALA 13 LEU 14 -0.0002

LEU 14 LEU 15 0.0001

LEU 15 LEU 16 -0.0003

LEU 16 LEU 17 0.0047

LEU 17 VAL 18 -0.0001

VAL 18 LEU 19 0.0001

LEU 19 SER 20 0.0004

SER 20 LEU 21 -0.0029

LEU 21 LEU 22 -0.0002

LEU 22 GLY 23 -0.0001

GLY 23 PHE 24 -0.0001

PHE 24 VAL 25 -0.0004

VAL 25 ILE 26 -0.0002

ILE 26 LEU 27 0.0000

LEU 27 LEU 28 -0.0001

LEU 28 ARG 29 -0.0141

ARG 29 ASP 30 -0.0000

ASP 30 PRO 31 0.0001

PRO 31 LEU 32 -0.0002

LEU 32 ASN 33 -0.0144

ASN 33 ALA 34 0.0002

ALA 34 ASN 35 -0.0001

ASN 35 LEU 36 -0.0001

LEU 36 VAL 37 0.0208

VAL 37 THR 38 0.0001

THR 38 GLN 39 0.0001

GLN 39 ASN 40 0.0001

ASN 40 ILE 41 -0.0216

ILE 41 TYR 42 -0.0000

TYR 42 ILE 43 -0.0002

ILE 43 GLY 44 -0.0000

GLY 44 TYR 45 -0.0316

TYR 45 PHE 46 0.0003

PHE 46 HIS 47 0.0003

HIS 47 TYR 48 0.0002

TYR 48 LEU 49 -0.0299

LEU 49 GLY 50 -0.0000

GLY 50 THR 51 0.0002

THR 51 LEU 52 -0.0000

LEU 52 LEU 53 0.0126

LEU 53 GLN 54 0.0001

GLN 54 GLY 55 0.0002

GLY 55 ASP 56 -0.0001

ASP 56 PHE 57 -0.0139

PHE 57 GLY 58 -0.0004

GLY 58 ILE 59 0.0004

ILE 59 THR 60 -0.0001

THR 60 TYR 61 -0.0151

TYR 61 ASN 62 -0.0001

ASN 62 GLY 63 0.0002

GLY 63 GLY 64 0.0002

GLY 64 LYS 65 -0.0096

LYS 65 SER 66 -0.0003

SER 66 LEU 67 -0.0000

LEU 67 MET 68 -0.0002

MET 68 ASN 69 0.0270

ASN 69 LEU 70 0.0002

LEU 70 ILE 71 -0.0001

ILE 71 LEU 72 -0.0002

LEU 72 THR 73 0.0311

THR 73 VAL 74 -0.0003

VAL 74 LEU 75 -0.0001

LEU 75 PRO 76 -0.0003

PRO 76 PRO 77 -0.0070

PRO 77 THR 78 0.0002

THR 78 LEU 79 -0.0002

LEU 79 GLU 80 -0.0000

GLU 80 LEU 81 0.0017

LEU 81 CYS 82 -0.0000

CYS 82 PHE 83 0.0003

PHE 83 ILE 84 0.0002

ILE 84 THR 85 0.0140

THR 85 LEU 86 0.0001

LEU 86 PHE 87 -0.0001

PHE 87 LEU 88 -0.0003

LEU 88 ALA 89 0.0033

ALA 89 PHE 90 -0.0001

PHE 90 ILE 91 0.0000

ILE 91 PHE 92 0.0000

PHE 92 GLY 93 0.0013

GLY 93 LEU 94 0.0003

LEU 94 PRO 95 -0.0002

PRO 95 LEU 96 -0.0002

LEU 96 GLY 97 0.0117

GLY 97 ILE 98 -0.0001

ILE 98 ILE 99 0.0001

ILE 99 SER 100 -0.0003

SER 100 ALA 101 0.0147

ALA 101 VAL 102 0.0002

VAL 102 ASN 103 -0.0005

ASN 103 SER 104 0.0000

SER 104 GLU 105 -0.0032

GLU 105 GLN 106 -0.0001

GLN 106 VAL 107 0.0004

VAL 107 PHE 108 0.0001

PHE 108 ALA 109 -0.0052

ALA 109 LYS 110 -0.0002

LYS 110 SER 111 0.0000

SER 111 LEU 112 0.0002

LEU 112 GLN 113 0.0079

GLN 113 ILE 114 -0.0001

ILE 114 LEU 115 0.0000

LEU 115 SER 116 0.0001

SER 116 TYR 117 0.0056

TYR 117 VAL 118 0.0002

VAL 118 GLY 119 0.0003

GLY 119 LEU 120 0.0001

LEU 120 SER 121 0.0016

SER 121 ILE 122 0.0000

ILE 122 PRO 123 -0.0001

PRO 123 ILE 124 -0.0001

ILE 124 PHE 125 0.0098

PHE 125 TRP 126 0.0001

TRP 126 LEU 127 -0.0001

LEU 127 ALA 128 -0.0000

ALA 128 PRO 129 0.0012

PRO 129 ILE 130 0.0000

ILE 130 LEU 131 0.0003

LEU 131 LEU 132 -0.0000

LEU 132 TYR 133 0.0090

TYR 133 VAL 134 0.0000

VAL 134 ALA 135 -0.0002

ALA 135 ALA 136 0.0001

ALA 136 LEU 137 0.0433

LEU 137 SER 138 -0.0002

SER 138 HIS 139 -0.0000

HIS 139 TRP 140 -0.0001

TRP 140 GLU 141 0.0545

GLU 141 ILE 142 0.0003

ILE 142 ALA 143 0.0004

ALA 143 ALA 144 -0.0002

ALA 144 ILE 145 0.0572

ILE 145 GLY 146 -0.0000

GLY 146 GLN 147 -0.0000

GLN 147 TYR 148 0.0002

TYR 148 ASN 149 -0.0039

ASN 149 LEU 150 -0.0002

LEU 150 LEU 151 0.0001

LEU 151 TYR 152 -0.0002

TYR 152 GLU 153 0.0156

GLU 153 ILE 154 -0.0003

ILE 154 LYS 155 0.0000

LYS 155 SER 156 0.0001

SER 156 ILE 157 0.0114

ILE 157 THR 158 -0.0000

THR 158 GLY 159 0.0002

GLY 159 PHE 160 -0.0002

PHE 160 PRO 161 -0.0187

PRO 161 VAL 162 -0.0002

VAL 162 ILE 163 0.0003

ILE 163 ASP 164 0.0000

ASP 164 MET 165 -0.0272

MET 165 TRP 166 -0.0002

TRP 166 PHE 167 0.0001

PHE 167 MET 168 0.0002

MET 168 GLU 169 -0.0204

GLU 169 VAL 170 -0.0002

VAL 170 PRO 171 -0.0002

PRO 171 TYR 172 0.0003

TYR 172 ARG 173 -0.0063

ARG 173 THR 174 -0.0004

THR 174 LYS 175 0.0004

LYS 175 ILE 176 -0.0001

ILE 176 VAL 177 -0.0061

VAL 177 GLN 178 -0.0001

GLN 178 ASN 179 -0.0001

ASN 179 ILE 180 0.0001

ILE 180 LEU 181 0.0049

LEU 181 GLN 182 0.0002

GLN 182 HIS 183 0.0002

HIS 183 LEU 184 0.0000

LEU 184 ALA 185 0.0033

ALA 185 LEU 186 -0.0004

LEU 186 PRO 187 0.0002

PRO 187 THR 188 0.0003

THR 188 LEU 189 0.0273

LEU 189 VAL 190 -0.0004

VAL 190 LEU 191 -0.0001

LEU 191 CYS 192 -0.0000

CYS 192 ILE 193 0.0163

ILE 193 LEU 194 0.0001

LEU 194 PRO 195 -0.0001

PRO 195 THR 196 0.0004

THR 196 MET 197 0.0083

MET 197 GLU 198 -0.0002

GLU 198 ILE 199 0.0003

ILE 199 ILE 200 -0.0003

ILE 200 ARG 201 0.0138

ARG 201 ILE 202 -0.0000

ILE 202 ILE 203 0.0002

ILE 203 HIS 204 0.0001

HIS 204 GLN 205 0.0141

GLN 205 ARG 206 0.0000

ARG 206 ALA 207 0.0001

ALA 207 GLU 208 0.0000

GLU 208 TYR 209 0.0185

TYR 209 ILE 210 0.0001

ILE 210 LEU 211 -0.0000

LEU 211 ASN 212 0.0001

ASN 212 GLN 213 0.0336

GLN 213 ASN 214 -0.0001

ASN 214 PHE 215 0.0002

PHE 215 SER 216 -0.0000

SER 216 LYS 217 0.0051

LYS 217 VAL 218 -0.0000

VAL 218 ALA 219 -0.0000

ALA 219 THR 220 0.0000

THR 220 THR 221 0.0152

THR 221 ARG 222 -0.0000

ARG 222 GLY 223 -0.0002

GLY 223 TRP 224 -0.0000

TRP 224 SER 225 0.0466

SER 225 LYS 226 0.0002

LYS 226 TRP 227 -0.0003

TRP 227 LYS 228 0.0004

LYS 228 ILE 229 -0.0086

ILE 229 LEU 230 0.0003

LEU 230 HIS 231 0.0002

HIS 231 GLN 232 -0.0003

GLN 232 TYR 233 0.0039

TYR 233 VAL 234 -0.0004

VAL 234 PHE 235 -0.0000

PHE 235 ARG 236 -0.0002

ARG 236 ASN 237 0.0006

ASN 237 THR 238 0.0000

THR 238 PHE 239 -0.0002

PHE 239 PRO 240 0.0001

PRO 240 LEU 241 0.0136

LEU 241 LEU 242 -0.0004

LEU 242 VAL 243 0.0002

VAL 243 PRO 244 -0.0000

PRO 244 GLN 245 -0.0017

GLN 245 VAL 246 -0.0001

VAL 246 PRO 247 -0.0001

PRO 247 ARG 248 0.0000

ARG 248 VAL 249 -0.0240

VAL 249 PHE 250 -0.0003

PHE 250 THR 251 0.0003

THR 251 LEU 252 -0.0004

LEU 252 VAL 253 -0.0033

VAL 253 LEU 254 -0.0001

LEU 254 THR 255 -0.0001

THR 255 GLN 256 0.0000

GLN 256 CYS 257 0.0212

CYS 257 MET 258 0.0000

MET 258 LEU 259 0.0004

LEU 259 VAL 260 0.0001

VAL 260 GLU 261 0.0118

GLU 261 THR 262 0.0002

THR 262 ALA 263 -0.0003

ALA 263 LEU 264 0.0000

LEU 264 GLY 265 0.0289

GLY 265 TRP 266 0.0000

TRP 266 PRO 267 -0.0001

PRO 267 GLY 268 -0.0002

GLY 268 ILE 269 0.0233

ILE 269 GLY 270 0.0002

GLY 270 ARG 271 -0.0000

ARG 271 TRP 272 0.0002

TRP 272 LEU 273 -0.0078

LEU 273 ILE 274 -0.0000

ILE 274 ASN 275 -0.0003

ASN 275 ALA 276 -0.0002

ALA 276 VAL 277 -0.0421

VAL 277 ASN 278 0.0002

ASN 278 GLU 279 0.0001

GLU 279 GLN 280 0.0002

GLN 280 ASP 281 -0.0248

ASP 281 TYR 282 -0.0001

TYR 282 ASN 283 0.0002

ASN 283 SER 284 0.0003

SER 284 ILE 285 -0.0088

ILE 285 ALA 286 0.0000

ALA 286 ALA 287 -0.0002

ALA 287 GLY 288 -0.0004

GLY 288 VAL 289 0.0093

VAL 289 ILE 290 -0.0000

ILE 290 VAL 291 0.0003

VAL 291 ILE 292 -0.0000

ILE 292 GLY 293 -0.0156

GLY 293 VAL 294 -0.0001

VAL 294 CYS 295 -0.0001

CYS 295 ILE 296 -0.0000

ILE 296 ILE 297 -0.0124

ILE 297 LEU 298 0.0002

LEU 298 ILE 299 -0.0003

ILE 299 ASP 300 0.0001

ASP 300 THR 301 -0.0031

THR 301 PHE 302 -0.0002

PHE 302 THR 303 -0.0000

THR 303 LYS 304 0.0002

LYS 304 ILE 305 0.0197

ILE 305 PHE 306 0.0001

PHE 306 THR 307 0.0002

THR 307 PHE 308 -0.0002

PHE 308 ILE 309 -0.0111

ILE 309 LEU 310 -0.0001

LEU 310 ASP 311 0.0001

ASP 311 PRO 312 -0.0001

PRO 312 PHE 313 -0.0066

PHE 313 LYS 314 -0.0001

LYS 314 LYS 315 -0.0002

LYS 315 LYS 316 0.0004

LYS 316 GLY 317 -0.1193

GLY 317 TRP 318 0.0002

TRP 318 TYR 319 0.0002

TYR 319 ALA 320 0.0002

ALA 320 LYS 321 -0.1591

LYS 321 MET 1 -0.8196

MET 1 GLN 2 0.0001

GLN 2 ASN 3 0.0001

ASN 3 LYS 4 0.0001

LYS 4 GLU 5 -0.3726

GLU 5 PRO 6 0.0000

PRO 6 ASP 7 0.0001

ASP 7 GLU 8 0.0000

GLU 8 PHE 9 -0.0289

PHE 9 ARG 10 0.0001

ARG 10 GLU 11 -0.0003

GLU 11 SER 12 -0.0001

SER 12 THR 13 0.3408

THR 13 SER 14 0.0003

SER 14 ILE 15 -0.0000

ILE 15 PHE 16 -0.0002

PHE 16 GLN 17 0.1815

GLN 17 ILE 18 0.0001

ILE 18 TRP 19 -0.0002

TRP 19 LEU 20 0.0003

LEU 20 ARG 21 -0.0112

ARG 21 PHE 22 -0.0001

PHE 22 ARG 23 -0.0000

ARG 23 GLN 24 0.0000

GLN 24 ASN 25 -0.0752

ASN 25 THR 26 -0.0002

THR 26 ILE 27 -0.0001

ILE 27 ALA 28 -0.0003

ALA 28 LEU 29 0.0037

LEU 29 PHE 30 0.0001

PHE 30 SER 31 -0.0002

SER 31 PHE 32 -0.0002

PHE 32 TYR 33 0.0123

TYR 33 LEU 34 0.0001

LEU 34 LEU 35 -0.0003

LEU 35 ILE 36 -0.0000

ILE 36 ALA 37 0.0291

ALA 37 LEU 38 -0.0000

LEU 38 ILE 39 -0.0001

ILE 39 PHE 40 0.0001

PHE 40 THR 41 0.0167

THR 41 ALA 42 -0.0001

ALA 42 LEU 43 0.0004

LEU 43 PHE 44 -0.0002

PHE 44 ALA 45 0.0053

ALA 45 SER 46 0.0002

SER 46 TYR 47 0.0000

TYR 47 LEU 48 -0.0002

LEU 48 ALA 49 0.0428

ALA 49 PRO 50 0.0001

PRO 50 TYR 51 -0.0001

TYR 51 ALA 52 0.0001

ALA 52 ASP 53 -0.0005

ASP 53 ASN 54 0.0004

ASN 54 ARG 55 0.0001

ARG 55 GLN 56 -0.0002

GLN 56 PHE 57 -0.0042

PHE 57 ILE 58 -0.0002

ILE 58 GLY 59 0.0000

GLY 59 GLN 60 -0.0003

GLN 60 GLU 61 0.0002

GLU 61 LEU 62 0.0002

LEU 62 MET 63 -0.0003

MET 63 PRO 64 0.0004

PRO 64 PRO 65 -0.0028

PRO 65 SER 66 -0.0003

SER 66 TRP 67 0.0000

TRP 67 VAL 68 -0.0002

VAL 68 ASP 69 0.0092

ASP 69 ARG 70 -0.0003

ARG 70 GLY 71 -0.0004

GLY 71 LYS 72 -0.0000

LYS 72 ILE 73 0.0077

ILE 73 ALA 74 -0.0000

ALA 74 PHE 75 0.0001

PHE 75 PHE 76 -0.0001

PHE 76 PHE 77 -0.0021

PHE 77 GLY 78 0.0002

GLY 78 THR 79 -0.0002

THR 79 ASP 80 0.0001

ASP 80 ASP 81 0.0010

ASP 81 LEU 82 0.0001

LEU 82 GLY 83 -0.0001

GLY 83 ARG 84 -0.0001

ARG 84 ASP 85 0.0027

ASP 85 ILE 86 0.0003

ILE 86 LEU 87 0.0005

LEU 87 SER 88 -0.0001

SER 88 ARG 89 0.0005

ARG 89 LEU 90 0.0002

LEU 90 ILE 91 0.0002

ILE 91 MET 92 0.0001

MET 92 GLY 93 0.0065

GLY 93 THR 94 0.0000

THR 94 ARG 95 0.0001

ARG 95 TYR 96 -0.0003

TYR 96 THR 97 0.0046

THR 97 LEU 98 0.0001

LEU 98 GLY 99 0.0000

GLY 99 SER 100 -0.0004

SER 100 ALA 101 0.0093

ALA 101 LEU 102 0.0002

LEU 102 LEU 103 -0.0003

LEU 103 VAL 104 0.0003

VAL 104 VAL 105 0.0017

VAL 105 PHE 106 -0.0000

PHE 106 SER 107 -0.0001

SER 107 VAL 108 -0.0003

VAL 108 ALA 109 0.0047

ALA 109 ILE 110 -0.0001

ILE 110 ILE 111 0.0004

ILE 111 GLY 112 -0.0003

GLY 112 GLY 113 -0.0046

GLY 113 ALA 114 0.0001

ALA 114 LEU 115 -0.0001

LEU 115 GLY 116 0.0001

GLY 116 ILE 117 0.0014

ILE 117 ILE 118 -0.0002

ILE 118 ALA 119 0.0002

ALA 119 GLY 120 0.0003

GLY 120 LEU 121 -0.0177

LEU 121 LEU 122 0.0003

LEU 122 LYS 123 0.0002

LYS 123 GLY 124 -0.0001

GLY 124 ILE 125 -0.0294

ILE 125 LYS 126 0.0001

LYS 126 ALA 127 0.0004

ALA 127 ARG 128 -0.0002

ARG 128 PHE 129 -0.0019

PHE 129 VAL 130 -0.0000

VAL 130 GLY 131 -0.0004

GLY 131 HIS 132 0.0000

HIS 132 ILE 133 0.0302

ILE 133 PHE 134 0.0001

PHE 134 ASP 135 0.0002

ASP 135 ALA 136 -0.0003

ALA 136 PHE 137 0.0137

PHE 137 LEU 138 -0.0003

LEU 138 SER 139 -0.0000

SER 139 LEU 140 0.0000

LEU 140 PRO 141 -0.0209

PRO 141 ILE 142 -0.0002

ILE 142 LEU 143 -0.0004

LEU 143 LEU 144 -0.0001

LEU 144 ILE 145 0.0064

ILE 145 ALA 146 0.0003

ALA 146 VAL 147 0.0001

VAL 147 VAL 148 0.0004

VAL 148 ILE 149 0.0036

ILE 149 SER 150 0.0004

SER 150 THR 151 -0.0004

THR 151 LEU 152 -0.0002

LEU 152 MET 153 0.0047

MET 153 GLU 154 0.0000

GLU 154 PRO 155 0.0001

PRO 155 SER 156 0.0002

SER 156 LEU 157 -0.0020

LEU 157 TRP 158 0.0002

TRP 158 ASN 159 -0.0001

ASN 159 ALA 160 0.0002

ALA 160 MET 161 -0.0009

MET 161 PHE 162 -0.0002

PHE 162 ALA 163 0.0003

ALA 163 THR 164 0.0002

THR 164 LEU 165 0.0015

LEU 165 LEU 166 -0.0003

LEU 166 ALA 167 -0.0001

ALA 167 ILE 168 -0.0004

ILE 168 LEU 169 -0.0012

LEU 169 PRO 170 -0.0000

PRO 170 TYR 171 -0.0001

TYR 171 PHE 172 -0.0001

PHE 172 ILE 173 0.0017

ILE 173 HIS 174 0.0003

HIS 174 THR 175 -0.0001

THR 175 ILE 176 -0.0001

ILE 176 TYR 177 0.0099

TYR 177 ARG 178 0.0001

ARG 178 ALA 179 -0.0002

ALA 179 ILE 180 0.0001

ILE 180 GLN 181 0.0257

GLN 181 LYS 182 -0.0001

LYS 182 GLU 183 0.0001

GLU 183 LEU 184 0.0003

LEU 184 GLU 185 0.0424

GLU 185 LYS 186 0.0004

LYS 186 ASP 187 -0.0001

ASP 187 TYR 188 -0.0000

TYR 188 VAL 189 -0.0099

VAL 189 VAL 190 -0.0002

VAL 190 MET 191 -0.0001

MET 191 LEU 192 -0.0002

LEU 192 LYS 193 -0.0035

LYS 193 LEU 194 -0.0003

LEU 194 GLU 195 -0.0003

GLU 195 GLY 196 0.0002

GLY 196 ILE 197 0.0378

ILE 197 SER 198 0.0001

SER 198 ASN 199 -0.0004

ASN 199 GLN 200 0.0002

GLN 200 ALA 201 0.0352

ALA 201 LEU 202 0.0001

LEU 202 LEU 203 0.0002

LEU 203 LYS 204 0.0001

LYS 204 SER 205 -0.0536

SER 205 THR 206 0.0002

THR 206 ILE 207 -0.0003

ILE 207 LEU 208 0.0002

LEU 208 PRO 209 -0.0023

PRO 209 ASN 210 0.0002

ASN 210 ILE 211 -0.0001

ILE 211 THR 212 -0.0000

THR 212 VAL 213 0.0389

VAL 213 ILE 214 -0.0006

ILE 214 TYR 215 -0.0000

TYR 215 ILE 216 -0.0001

ILE 216 GLN 217 0.0272

GLN 217 GLU 218 -0.0004

GLU 218 VAL 219 0.0002

VAL 219 ALA 220 -0.0000

ALA 220 ARG 221 0.0121

ARG 221 ALA 222 0.0000

ALA 222 PHE 223 -0.0003

PHE 223 VAL 224 -0.0002

VAL 224 ILE 225 -0.0082

ILE 225 ALA 226 -0.0001

ALA 226 VAL 227 0.0000

VAL 227 LEU 228 -0.0001

LEU 228 ASP 229 -0.0015

ASP 229 ILE 230 -0.0001

ILE 230 SER 231 -0.0004

SER 231 ALA 232 0.0001

ALA 232 LEU 233 0.0021

LEU 233 SER 234 0.0002

SER 234 PHE 235 0.0001

PHE 235 ILE 236 -0.0001

ILE 236 SER 237 0.0060

SER 237 LEU 238 -0.0003

LEU 238 GLY 239 0.0003

GLY 239 ALA 240 0.0002

ALA 240 GLN 241 -0.0057

GLN 241 ARG 242 0.0002

ARG 242 PRO 243 -0.0000

PRO 243 THR 244 -0.0003

THR 244 PRO 245 0.0009

PRO 245 GLU 246 0.0001

GLU 246 TRP 247 0.0001

TRP 247 GLY 248 -0.0001

GLY 248 ALA 249 0.0015

ALA 249 MET 250 0.0001

MET 250 ILE 251 0.0001

ILE 251 LYS 252 -0.0001

LYS 252 ASP 253 -0.0190

ASP 253 SER 254 0.0001

SER 254 LEU 255 0.0001

LEU 255 GLU 256 0.0002

GLU 256 LEU 257 -0.0109

LEU 257 LEU 258 0.0002

LEU 258 TYR 259 -0.0001

TYR 259 LEU 260 -0.0002

LEU 260 ALA 261 0.0095

ALA 261 PRO 262 0.0002

PRO 262 TRP 263 0.0001

TRP 263 THR 264 0.0001

THR 264 VAL 265 -0.0009

VAL 265 LEU 266 -0.0002

LEU 266 LEU 267 0.0002

LEU 267 PRO 268 -0.0001

PRO 268 GLY 269 0.0004

GLY 269 PHE 270 0.0000

PHE 270 ALA 271 -0.0000

ALA 271 ILE 272 0.0003

ILE 272 ILE 273 -0.0008

ILE 273 PHE 274 -0.0004

PHE 274 THR 275 -0.0001

THR 275 ILE 276 -0.0000

ILE 276 LEU 277 -0.0063

LEU 277 LEU 278 -0.0001

LEU 278 SER 279 -0.0001

SER 279 ILE 280 0.0002

ILE 280 ILE 281 -0.0093

ILE 281 PHE 282 -0.0001

PHE 282 SER 283 -0.0003

SER 283 ASN 284 0.0002

ASN 284 GLY 285 -0.0048

GLY 285 LEU 286 0.0000

LEU 286 THR 287 -0.0000

THR 287 LYS 288 0.0002

LYS 288 ALA 289 0.0065

ALA 289 ILE 290 0.0001

ILE 290 ASN 291 0.0002

ASN 291 GLN 292 -0.0002

GLN 292 HIS 293 0.0305

HIS 293 GLN 294 -0.0000

GLN 294 GLU 295 0.0001

If you find results from this site helpful for your research, please cite one of our papers:

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 8th, 2025.

Should you encounter any unexpected behaviour, please let us know.

*** NMA2BCoF ***

CA strain for 2502181855492627392

--- normal mode 25 ---

Should you encounter any unexpected behaviour,
please let us know.

* NMA2BCoF *